The plasticity of human skeletal muscle, with regard to growth and atrophy, continues to be of great interest, especially in the areas of medicine, sports and nutrition. Additionally, the study of patients' catabolic conditions, especially in clinical and/or hospital situations, including prolonged bed rest, human immunodeficiency virus, post trauma (i.e., burns, surgery) and hormonal disorders (i.e., Cushing's Syndrome), the loss of body weight and/or the loss of muscle protein is of particular importance. As observed in catabolic conditions, muscle protein degradation normally exceeds muscle protein synthesis, which is a concern the present invention addresses.
Skeletal muscle hypertrophy or growth is characterized by gains in myofibrillar mass and muscle fiber hyperplasia, as discussed by J. Antonio and W. Gonyea, "Muscle Fiber Splitting In Stretch-Enlarged Avian Muscle," Medicine and Science in Sports and Exercise, Vol. 26, No. 8, pp. 973-977, 1994. Strenuous resistance exercise has been shown to promote the elevation of muscle protein synthesis rates for a period of up to 24 hours, after the completion of the exercise. Possible explanations for this hypertrophic response include: elevated levels of anabolic hormones (i.e., testosterone, growth hormone, insulin-like growth factor), muscle stretch, and an overcompensation of protein synthesis to repair injured or damaged muscle tissue. Additionally, it is well known that many athletes eat frequent meals throughout the day in an attempt to maintain skeletal muscle in a continuous anabolic state.
Although the precise mechanism for increased protein synthesis is not completely understood, it is apparent that amino acids must be available for there to be a net increase in muscle protein. In essence, protein intake is critical in the etiology of skeletal muscle hypertrophy. Simply providing protein, regardless of its source, may not be the most effective way of promoting the anabolic environment or drive in exercise-trained skeletal muscle. In terms of bioavailability, animal sources of protein are superior to plant sources of protein.
The recommended dietary intake (RDI) for protein is 0.8 grams/kg body weight per day. However, it has been demonstrated that in resistance-trained athletes, the intake for protein should be approximately twice the normal RDI (1.5-2.0 grams/kg body weight per day), P. W. Lemon, "Protein And Amino Acid Needs Of The Strength Athlete," International Journal of Sport Nutrition, Vol. 1, No. 2, pp. 127-145, 1991. One preferred source of animal protein is dairy whey. Additionally, the results of weight gain and nitrogen retention, both important in muscle building, are improved using whey protein hydrolysate, as compared to using whole proteins. M. Poullain et al., "Effect Of Whey Proteins, Their Oligopeptide Hydrolysates and Free Amino Acid Mixtures on Growth and Nitrogen Retention in Fed and Starved Rats," Journal of Parental and Enteral Nutrition, Vol. 13, No. 4, pp. 382-386, 1989. Conversely, the use of free amino acid mixtures appear to be the least effective means for weight gain and/or nitrogen retention. Thus, it has now been discovered that a novel process for making liposomal, ion-exchange whey protein and introducing it into the body, results in the sustained release of amino acids, which promotes an increase in muscle mass and offsets certain catabolic conditions.
Although the need for such process of making a liposomal ion-exchange whey protein and the products thereof, have been long felt, the prior art, heretofore, has not provided such a process and/or product which meets all of the aforementioned criterion.
Additional features and advantages of the invention will be set forth in part in the description which follows, and in part will become apparent from the description, or may be learned by practice of the invention. The features and advantages of the invention may be realized by means of the combinations and steps particularly pointed out in the appended claims.